Entry STF0013
Equine lysozyme
Protein information
Name of the protein: | Lysozyme C, milk isozyme |
Organism: | Equus caballus |
Number of residues: | 129 |
Related UniProt entry: | P11376 (Fragment: 1 - 129) |
Related PDB entry: | 2EQL |
Visualize the data
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Experiment sets
EARLY
Method: HDX-folding competition by NMR
Conditions: pH 7.5; 25.0 Celsius; Probes: 46 amides + 3 Trp indole hydrogen atoms
Related publication:
PMID 10369782
Experiment details: "Equine lysozyme denatured in 6 M GdnHCl was diluted rapidly with deuterated buffer solution at pH 7.5 and 25 °C, in order to initiate simultaneous hydrogen exchange and protein refolding. The intrinsic time constants for amide hydrogen exchange under these conditions are of the order of 10-200 ms. Exchange was allowed to occur for one minute, and was then quenched by decreasing the pH to 4.5."
Protection threshold: strong protection within 3.5 ms
Sequence:
KVFSKCELAHKLKAQEMDGFGGYSLANWVCMAEYESNFNTRAFNGKNANGSSDYGLFQLNNKWWCKDNKRSSSNACNIMCSKLLDENIDDDISCAKRVVRDPKGMSAWKAWVKHCKDKDLSEYLASCNL
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EARLY residues
8: L;
9: A;
11: K;
12: L;
13: K;
28: W;
29: V;
31: M;
111: W;
115: C;
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INTERMEDIATE
Method: HDX-folding competition by NMR
Conditions: pH 7.5; 25.0 Celsius; Probes: 46 amides + 3 Trp indole hydrogen atoms
Related publication:
PMID 10369782
Experiment details: "Equine lysozyme denatured in 6 M GdnHCl was diluted rapidly with deuterated buffer solution at pH 7.5 and 25 °C, in order to initiate simultaneous hydrogen exchange and protein refolding. The intrinsic time constants for amide hydrogen exchange under these conditions are of the order of 10-200 ms. Exchange was allowed to occur for one minute, and was then quenched by decreasing the pH to 4.5."
Protection threshold: strong protection within 10 ms
Sequence:
KVFSKCELAHKLKAQEMDGFGGYSLANWVCMAEYESNFNTRAFNGKNANGSSDYGLFQLNNKWWCKDNKRSSSNACNIMCSKLLDENIDDDISCAKRVVRDPKGMSAWKAWVKHCKDKDLSEYLASCNL
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INTERMEDIATE residues
15: Q;
23: Y;
27: N;
34: Y;
35: E;
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LATE
Method: HDX-folding competition by NMR
Conditions: pH 7.5; 25.0 Celsius; Probes: 46 amides + 3 Trp indole hydrogen atoms
Related publication:
PMID 10369782
Experiment details: "Equine lysozyme denatured in 6 M GdnHCl was diluted rapidly with deuterated buffer solution at pH 7.5 and 25 °C, in order to initiate simultaneous hydrogen exchange and protein refolding. The intrinsic time constants for amide hydrogen exchange under these conditions are of the order of 10-200 ms. Exchange was allowed to occur for one minute, and was then quenched by decreasing the pH to 4.5."
Protection threshold: strong protection within 50 ms
Sequence:
KVFSKCELAHKLKAQEMDGFGGYSLANWVCMAEYESNFNTRAFNGKNANGSSDYGLFQLNNKWWCKDNKRSSSNACNIMCSKLLDENIDDDISCAKRVVRDPKGMSAWKAWVKHCKDKDLSEYLASCNL
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LATE residues
4: S;
38: F;
61: N;
108: W;
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STRONG
Method: Native exchange NMR
Conditions: pH 4.5; 25.0 Celsius; Probes: 67
Related publication:
PMID 9180380
Experiment details: "Samples for hydrogen exchange studies of the native holo state of equine lysozyme were adjusted to pH 4.5 in H2O and freeze-dried. The protein was then dissolved in D2O in the presence of 10 mM CaCl2, and the apparent pH adjusted to 4.5 using 2HCl and NaO2H. Samples were allowed to undergo exchange at 25 °C for time intervals ranging from a few minutes to 63 days. At the end of each exchange period, phase-sensitive COSY spectra were acquired."
Protection threshold: log(P) > 5
Sequence:
KVFSKCELAHKLKAQEMDGFGGYSLANWVCMAEYESNFNTRAFNGKNANGSSDYGLFQLNNKWWCKDNKRSSSNACNIMCSKLLDENIDDDISCAKRVVRDPKGMSAWKAWVKHCKDKDLSEYLASCNL
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STRONG residues
9: A;
11: K;
12: L;
13: K;
27: N;
28: W;
31: M;
32: A;
38: F;
39: N;
61: N;
65: C;
93: S;
94: C;
95: A;
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MEDIUM
Method: Native exchange NMR
Conditions: pH 4.5; 25.0 Celsius; Probes: 67
Related publication:
PMID 9180380
Experiment details: "Samples for hydrogen exchange studies of the native holo state of equine lysozyme were adjusted to pH 4.5 in H2O and freeze-dried. The protein was then dissolved in D2O in the presence of 10 mM CaCl2, and the apparent pH adjusted to 4.5 using 2HCl and NaO2H. Samples were allowed to undergo exchange at 25 °C for time intervals ranging from a few minutes to 63 days. At the end of each exchange period, phase-sensitive COSY spectra were acquired."
Protection threshold: 4 < log(P) < 5
Sequence:
KVFSKCELAHKLKAQEMDGFGGYSLANWVCMAEYESNFNTRAFNGKNANGSSDYGLFQLNNKWWCKDNKRSSSNACNIMCSKLLDENIDDDISCAKRVVRDPKGMSAWKAWVKHCKDKDLSEYLASCNL
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MEDIUM residues
8: L;
10: H;
29: V;
33: E;
34: Y;
35: E;
36: S;
37: N;
40: T;
42: A;
54: Y;
57: F;
58: Q;
59: L;
62: K;
63: W;
66: K;
83: L;
96: K;
111: W;
112: V;
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